Publication

The role of (auto)-phosphorylation in the complex activation mechanism of LRRK2

Athanasopoulos, P. S., Heumann, R. & Kortholt, A., Jul-2018, In : Biological Chemistry. 399, 7, p. 643-647 5 p.

Research output: Contribution to journalArticleAcademicpeer-review

Mutations in human leucine-rich-repeat kinase 2 (LRRK2) have been found to be the most frequent cause of late-onset Parkinson's Disease (PD). LRRK2 is a large protein with two enzymatic domains, a GTPase and a kinase domain. A cluster of (auto)-phosphorylation sites within the N-terminus of LRRK2 have been shown to be crucial for the localization of LRRK2 and is important for PD pathogenesis. In addition, phosphorylation of sites within the G-domain of the protein affect GTPase activity. Here we discuss the role of these (auto)-phosphorylation sites of LRRK2 and their regulation by phosphatases and upstream kinases.

Original languageEnglish
Pages (from-to)643-647
Number of pages5
JournalBiological Chemistry
Volume399
Issue number7
Early online date12-Mar-2018
Publication statusPublished - Jul-2018
EventConference on Molecular Basis of Life - Bochum, Germany
Duration: 1-Sep-2017 → …

Event

Conference on Molecular Basis of Life

01/09/2017 → …

Bochum, Germany

Event: Conference

    Keywords

  • GTPase, kinase, neuronal degeneration, Parkinson's disease, phosphatases, DISEASE-ASSOCIATED MUTATIONS, SYNAPTIC VESICLE TRAFFICKING, REPEAT KINASE 2, PARKINSONS-DISEASE, GTP-BINDING, CYTOPLASMIC LOCALIZATION, PHOSPHORYLATION, PENETRANCE, PHENOTYPE, PROTEINS

View graph of relations

Download statistics

No data available

ID: 55482327